Soybean lioxygenase (SLO) has emerged as a paradigmatic system in which to study the role of hydrogen tunneling and its link to protein structure and dynamics. The proton-coupled electron transfer reaction, catalyzed by SLO, can be modeled using a multi-dimensional tunneling expression that is both electronically and vibrationally non-adiabtic. The suitability of this model has been critically tested by generating a double mutant that both expands the size of the enzyme active site and concomitantly rigidifies the protein. These studies provide a quantitative assessment of the importance of a close donor-acceptor distance (DAD) that can be achieved either by local DAD distance sampling or by more remote changes in the protein conformational landscape. Recent hydrogen/deuterium exchange experiments of the wild type and double mutant of SLO are uncovering a dynamical network of residues that leads from the outside of the protein to the active site.<br/>(Supported by the NIH, GM025765)

Tunneling and the role of barrier width in enzymatic C-H activation

249th National Meeting (2015)

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